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treatment of AtGSNOR with peroxynitrite, known as tyrosine nitrating agent, modifies this enzyme and inhibits its activity
-
peroxynitrite inhibits cytosolic NADP-ME2 activity due to tyrosine nitration at Tyr-73 to 3-nitrotyrosine
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causes a 26% inhibition in enzyme activity with 5 mM SIN-1
-
ethanol toxicity is mediated by peroxynitrite and the peroxynitrite-mediated damage to NADP+-dependent isocitrate dehydrogenase and superoxide dismutase may be resulting in the perturbation of the cellular antioxidant defense systems and subsequently lead to a pro-oxidant condition
-
excess of peroxynitrite inactivates the enzyme by overoxidation
-
50% inhibition at 0.032 mM in absence, at 0.153 mM in presence of 2-mercaptoethanol
-
almost complete inhibition via nitration of active-site residue Y34, no significant change in conformation upon nitration. Inhibition occurs either through a steric effect of 3-nitrotyrosine 34 that impedes substrate binding or through an electrostatic effect of the nitro group
-
0.1 mM, 50% inhibition of cysteine-free mutant C85S/C152E, no inhibition of wild-type
-
exclusively nitrates residues Tyr213, Try292, and Tyr345. Tyr345 is found at 3.3 A of His313, which is involved in the NADP-binding site. Nitration of residue Tyr345 is responsible for inhibition
-
40% inhibition of activity with 0.1 mM, 72% inhibition of activity with 0.2 mM
-
inactivation by modification of Tyr114 and Tyr106
-
inactivation of enzyme by formation of nitrotyrosine near the catalytic center, 2.5fold increased Km-value and 1.7fold decreased Vmax, molecular modeling
-
rapid and irreversible inactivation
-
inactivates isozyme NAT1, in vivo effect, overview
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inhibition is caused by oxidation at the active site cysteine
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1 mM, almost complete inactivation. After the exposure to 1 mM peroxynitrite, the molar content of Cys residues decreases from 8.63 to 3.43 and 4.24 in the absence and in the presence of bicarbonate, respectively. The addition of 1 mM DTT in 10 min after peroxynitrite treatment does not significantly reverse loss of either activity or molar content of DTNB-reactive Cys residues. No involvement of Tyr613 nitration in the control of enzymatic function. The enzymatic activity does not directly correlate with the protein nitration levels
-
the peroxynitrite-dependent inactivation of the enzyme could be due to the nitration of Tyr613, a key amino acid of the allosteric inhibitor site of the enzyme. Glycogen phosphorylase functions may be regulated by tyrosine nitration
-
nitrating conditions after exposure to peroxynitrite strongly inhibit enzyme activity. Among the isoforms, cytosolic OASA1 is markedly sensitive to nitration. Nitration assays on purified recombinant OASA1 protein lead to 90% reduction of the activity due to inhibition of the enzyme. Inhibition of OASA1 activity upon nitration correlates with the identification of a modified OASA1 protein containing a 3-nitroTyr302 residue. Inhibition caused by Tyr302 nitration on OASA1 activity seems to be due to a drastically reduced O-acetylserine substrate binding to the nitrated protein, and also to reduced stabilization of the pyridoxal-5-phosphate cofactor through hydrogen bonds
-
irreversible inhibition of nSMase1
-
causes nitration on several tyrosine residues including Tyr383 and Tyr466
-
in isolated nonsynaptic brain mitochondria Lon protease is highly susceptible to oxidative inactivation by peroxynitrite. This susceptibility is more pronounced with regard to ATP-stimulated activity, which is inhibited by 75% in the presence of a bolus addition of 1 mM ONOO, whereas basal unstimulated activity is inhibited by 45%. A decline in Lon protease activity precedes electron transport chain dysfunction and ATP-stimulated activity is approximately fivefold more sensitive than basal Lon protease activity. Supplementation of mitochondrial matrix extracts with reduced glutathione, following peroxynitrite exposure, results in partial restoration of basal and ATP-stimulated activity
-
50% inhibition at 280 microM and an enzyme concentration of 10 microM
-
0.01 mM, 50% inhibition
-
formation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13 a prothrombotic mechanism in diseases associated with oxidative stress, overview. Oxidation by peroxynitrite of purified VWF multimers inhibits ADAMTS-13 hydrolysis, but does not alter their electrophoretic pattern nor their ability to induce platelet agglutination by ristocetin. In vitro treatment of ADAMTS-13 with peroxynitrite over a concentration ranging from 0.050 to 0.250 mM causes a complete inhibition of the protease activity of the enzyme
-
activity of wild-type enzyme is reduced to 38% in presence of peroxynitrite. Activities of mutants Y153A and Y253A are 233 completely abolished in the presence of peroxynitrite. Mutant Y146A shows 32% reduction in activity
-
inhibition of 15% after exposure to peroxynitrite at concentrations ranging from 0.01-0.1 mM, 25% inhibition at 1 mM
-
0.1 mM, 50% inhibition, almost complete inhibition above 1 mM, nitration of tyrosine residues
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decrease of Vmax and KM for fructose-1,6-bisphosphate after incubation with peroxynitrite. Tyrosine residues in the carboxyl-terminal region of the aldolase are major targets of nitration. Tyrosine nitration of aldolase A can contribute to an impaired cellular glycolytic activity
-
exposure to peroxynitrite does not modify bound pyridoxal 5'-phosphate but leads to nitration of Trp208, Trp43 and Tyr223 and alterations in the heme environment including loss of thiolate coordination, conversion to high-spin and bleaching, with no detectable formation of oxoferryl compounds nor promotion of one-electron processes
-
i.e. ONOO-. 0.03-3 mM L-Cys, 0.03-3 mM glutathione, or 0.1-3 mM N-(2-mercaptopropionyl)glycine protects. 1 mM FeSO4 markedly enhances the protection provided by L-Cys, but not by glutathione or N-(2-mercaptopropionyl)glycine
-
inactivation due to the release of iron from the Fe-S cluster, other nitric oxide sources decrease the activity of the mitochondrial isozyme
-
reacts with [4Fe-4S] cluster yielding an inactive [3Fe-4S] enzyme. Carbon dioxide enhances the reaction. Peroxynitrite also induces aconitase tyrosine nitration, without contributing to inactivation
-
inhibits PGIS activity by nitration of Tyr 430
-
inhibits PGIS activity by nitration of tyrosine 430
-
substrate analog U46619 partially prevents inhibition
-
0.005 mM, activity is decreased by about 25%
-
0.005 mM, inactivation of the enzyme
-
inhibition of isozyme MtGS1a
-
CPS1 activity is decreased by treatment with peroxynitrite in a peroxynitrite concentration- and time-dependent manner due to tyrosine nitration (47% decrease in 1 min and 60% decrease in 10 min with 1 mM peroxynitrite)
-
addition of ONOO- to cytochrome bd in turnover with ascorbate and N,N,N',N'-tetramethyl-p-phenylenediamine causes the irreversible inhibition of about 15% of the enzyme fraction, due to the NO radical generated from ONOO-. Addition of ONOO- to cells expressing cytochrome bd as the only terminal oxidase, causes about 5% irreversible inhibition of O2 consumption. Purified cytochrome bd in turnover with O2 is able to metabolize ONOO- with an apparent turnover rate as high as about 10 mol ONOO- per mol of enzyme and per s at 25°C
-
0.1 mM, complete inhibition
-
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